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ADP-ribose pyrophosphatase

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Line 17: Line 17:
**[[1q33]] – hADPRP NUDT9 residues 59-350 – human<br />
**[[1q33]] – hADPRP NUDT9 residues 59-350 – human<br />
-
**[[1v8i]], [[3x0i]], [[3x0j]] - TtADPRP – ''Thermus thermophilus''<br />
+
**[[1v8i]], [[3x0i]], [[3x0j]], [[3x0l]], [[3x0n]], [[3x0p]], [[3x0q]], [[3x0s]] - TtADPRP – ''Thermus thermophilus''<br />
**[[3x0k]], [[3k0l]] - TtADPRP ES-state <br />
**[[3x0k]], [[3k0l]] - TtADPRP ES-state <br />
**[[3x0m]], [[3k0n]] - TtADPRP ESM-state <br />
**[[3x0m]], [[3k0n]] - TtADPRP ESM-state <br />

Revision as of 10:59, 22 February 2017

ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, 1khz

Drag the structure with the mouse to rotate

3D structures of ADP-ribose pyrophosphatase

Updated on 22-February-2017


References

  1. ↑ Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat Struct Biol. 2001 May;8(5):467-72. PMID:11323725 doi:10.1038/87647
  2. ↑ Gabelli SB, Bianchet MA, Ohnishi Y, Ichikawa Y, Bessman MJ, Amzel LM. Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase. Biochemistry. 2002 Jul 30;41(30):9279-85. PMID:12135348

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Michal Harel, Alexander Berchansky

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